Because of their rapid growth and their affordability, bacterial expression systems are very convenient when producing recombinant proteins.

Nevertheless, one of the key elements in the design of the experimental procedures for producing a recombinant protein in E. Coli is the selection of the right bacterial strain for the right protein. This is not an easy step but remains of utmost importance.

Based on our in-house experience, we’ve compiled a guide aimed at helping you in your choice of the “ideal” engineered bacterial strain for efficient recombinant proteins expression.

Pharmaceutical, biotech and medical device industries apply restrictive quality systems in their bio-production processes. Among the numerous parameters controlled daily by scientists, I have selected a particular one for this post, i.e endotoxin detection.

Isolation of highly purified untagged proteins is crucial in today’s R&D programs. Up to now, recombinant protein production approaches were often based on the use of “tags” to make protein purification (and solubility) more convenient. Unfortunately, these tags can be real experimental hurdles in downstream applications. Protein experts are now considering “tag-free” alternatives (including outsourcing) for producing untagged proteins more rapidly, more efficiently, and without jeopardizing the rest of the research project. Let’s see how this is possible.